eF-site ID 6av6-A PDB Code 6av6 Chain A click to enlarge Title Structure of human endothelial nitric oxide synthase heme domain in complex with 6-(3-Fluoro-5-(3-(methylamino)propyl)phenethyl)-4-methylpyridin-2-amine Classification OXIDOREDUCTASE Compound Nitric oxide synthase, endothelial Source (NOS3_HUMAN) Sequence A:  FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPR PEQLLSQARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAA TGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDAR DCRSAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRG DFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGW TPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPT LEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMS TEIGTRNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAA VEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARG GCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDP W Description Functional site 1) chain A residue 178 type sequence W description binding site for residue HEM A 501 source : AC1 2) chain A residue 184 type sequence C description binding site for residue HEM A 501 source : AC1 3) chain A residue 226 type sequence S description binding site for residue HEM A 501 source : AC1 4) chain A residue 353 type sequence F description binding site for residue HEM A 501 source : AC1 5) chain A residue 354 type sequence S description binding site for residue HEM A 501 source : AC1 6) chain A residue 356 type sequence W description binding site for residue HEM A 501 source : AC1 7) chain A residue 361 type sequence E description binding site for residue HEM A 501 source : AC1 8) chain A residue 447 type sequence W description binding site for residue HEM A 501 source : AC1 9) chain A residue 475 type sequence Y description binding site for residue HEM A 501 source : AC1 10) chain A residue 105 type sequence F description binding site for residue W68 A 502 source : AC2 11) chain A residue 336 type sequence V description binding site for residue W68 A 502 source : AC2 12) chain A residue 353 type sequence F description binding site for residue W68 A 502 source : AC2 13) chain A residue 356 type sequence W description binding site for residue W68 A 502 source : AC2 14) chain A residue 357 type sequence Y description binding site for residue W68 A 502 source : AC2 15) chain A residue 361 type sequence E description binding site for residue W68 A 502 source : AC2 16) chain A residue 322 type sequence W description binding site for residue BTB A 503 source : AC3 17) chain A residue 382 type sequence C description binding site for residue BTB A 503 source : AC3 18) chain A residue 384 type sequence D description binding site for residue BTB A 503 source : AC3 19) chain A residue 377 type sequence E description binding site for residue BTB A 504 source : AC4 20) chain A residue 387 type sequence T description binding site for residue BTB A 504 source : AC4 21) chain A residue 388 type sequence R description binding site for residue BTB A 504 source : AC4 22) chain A residue 94 type sequence C description binding site for residue ZN A 505 source : AC5 23) chain A residue 99 type sequence C description binding site for residue ZN A 505 source : AC5 24) chain A residue 167 type sequence E description binding site for residue GOL A 506 source : AC6 25) chain A residue 247 type sequence Q description binding site for residue CL A 507 source : AC7 26) chain A residue 357 type sequence Y description binding site for residue CL A 507 source : AC7 27) chain A residue 366 type sequence N description binding site for residue CL A 507 source : AC7 28) chain A residue 102 type sequence S description binding site for residue H4B B 501 source : AC9 29) chain A residue 365 type sequence R description binding site for residue H4B B 501 source : AC9 30) chain A residue 446 type sequence A description binding site for residue H4B B 501 source : AC9 31) chain A residue 447 type sequence W description binding site for residue H4B B 501 source : AC9 32) chain A residue 445 type sequence W description binding site for residue H4B B 503 source : AD2 33) chain A residue 460 type sequence F description binding site for residue H4B B 503 source : AD2 34) chain A residue 463 type sequence E description binding site for residue H4B B 503 source : AD2 35) chain A residue 261 type sequence V description binding site for residue BTB D 504 source : AF3 36) chain A residue 373 type sequence Y description binding site for residue BTB D 504 source : AF3 37) chain A residue 374 type sequence N description binding site for residue BTB D 504 source : AF3 38) chain A residue 378 type sequence D description binding site for residue BTB D 504 source : AF3 39) chain A residue 184 type catalytic sequence C description 935 source MCSA : MCSA1 40) chain A residue 187 type catalytic sequence R description 935 source MCSA : MCSA1 41) chain A residue 356 type catalytic sequence W description 935 source MCSA : MCSA1 42) chain A residue 361 type catalytic sequence E description 935 source MCSA : MCSA1 43) chain A residue 102 type BINDING sequence S description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 44) chain A residue 475 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 45) chain A residue 247 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 46) chain A residue 356 type BINDING sequence W description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 47) chain A residue 357 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 48) chain A residue 361 type BINDING sequence E description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 49) chain A residue 366 type BINDING sequence N description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 50) chain A residue 446 type BINDING sequence A description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 51) chain A residue 447 type BINDING sequence W description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 52) chain A residue 460 type BINDING sequence F description BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI2 53) chain A residue 184 type BINDING sequence C description axial binding residue => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O source Swiss-Prot : SWS_FT_FI3 54) chain A residue 183-190 type prosite sequence RCVGRIQW description NOS Nitric oxide synthase (NOS) signature. RCVGRIqW source prosite : PS60001 55) chain A residue 365 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P source Swiss-Prot : SWS_FT_FI4 56) chain A residue 94 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:18849972, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:1M9J, ECO:0007744|PDB:1M9K, ECO:0007744|PDB:1M9M, ECO:0007744|PDB:1M9Q, ECO:0007744|PDB:1M9R, ECO:0007744|PDB:3EAH, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P source Swiss-Prot : SWS_FT_FI1 57) chain A residue 99 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:18849972, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:1M9J, ECO:0007744|PDB:1M9K, ECO:0007744|PDB:1M9M, ECO:0007744|PDB:1M9Q, ECO:0007744|PDB:1M9R, ECO:0007744|PDB:3EAH, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P source Swiss-Prot : SWS_FT_FI1

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